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Database: UniProt
Entry: A0A1H8B325_9SPHN
LinkDB: A0A1H8B325_9SPHN
Original site: A0A1H8B325_9SPHN 
ID   A0A1H8B325_9SPHN        Unreviewed;       351 AA.
AC   A0A1H8B325;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Ribonucleoside-diphosphate reductase subunit beta {ECO:0000256|PIRNR:PIRNR000355};
DE            EC=1.17.4.1 {ECO:0000256|PIRNR:PIRNR000355};
GN   ORFNames=SAMN05192583_1183 {ECO:0000313|EMBL:SEM77360.1};
OS   Sphingomonas gellani.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=1166340 {ECO:0000313|EMBL:SEM77360.1, ECO:0000313|Proteomes:UP000199206};
RN   [1] {ECO:0000313|Proteomes:UP000199206}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S6-262 {ECO:0000313|Proteomes:UP000199206};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Provides the precursors necessary for DNA synthesis.
CC       Catalyzes the biosynthesis of deoxyribonucleotides from the
CC       corresponding ribonucleotides. {ECO:0000256|PIRNR:PIRNR000355}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[thioredoxin]-disulfide + a 2'-deoxyribonucleoside 5'-
CC         diphosphate + H2O = [thioredoxin]-dithiol + a ribonucleoside 5'-
CC         diphosphate; Xref=Rhea:RHEA:23252, Rhea:RHEA-COMP:10698, Rhea:RHEA-
CC         COMP:10700, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058,
CC         ChEBI:CHEBI:57930, ChEBI:CHEBI:73316; EC=1.17.4.1;
CC         Evidence={ECO:0000256|PIRNR:PIRNR000355};
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC         Evidence={ECO:0000256|PIRNR:PIRNR000355,
CC         ECO:0000256|PIRSR:PIRSR000355-2};
CC       Note=Binds 2 iron ions per subunit. {ECO:0000256|PIRNR:PIRNR000355,
CC       ECO:0000256|PIRSR:PIRSR000355-2};
CC   -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase small
CC       chain family. {ECO:0000256|ARBA:ARBA00009303,
CC       ECO:0000256|PIRNR:PIRNR000355}.
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DR   EMBL; FOCF01000002; SEM77360.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H8B325; -.
DR   STRING; 1166340.SAMN05192583_1183; -.
DR   OrthoDB; 9766544at2; -.
DR   UniPathway; UPA00326; -.
DR   Proteomes; UP000199206; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor; IEA:UniProtKB-EC.
DR   GO; GO:0009263; P:deoxyribonucleotide biosynthetic process; IEA:UniProtKB-KW.
DR   CDD; cd01049; RNRR2; 1.
DR   Gene3D; 1.10.620.20; Ribonucleotide Reductase, subunit A; 1.
DR   InterPro; IPR009078; Ferritin-like_SF.
DR   InterPro; IPR012348; RNR-like.
DR   InterPro; IPR033909; RNR_small.
DR   InterPro; IPR000358; RNR_small_fam.
DR   PANTHER; PTHR23409; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE SMALL CHAIN; 1.
DR   PANTHER; PTHR23409:SF18; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE SUBUNIT M2; 1.
DR   Pfam; PF00268; Ribonuc_red_sm; 1.
DR   PIRSF; PIRSF000355; NrdB; 1.
DR   SUPFAM; SSF47240; Ferritin-like; 1.
PE   3: Inferred from homology;
KW   Deoxyribonucleotide synthesis {ECO:0000256|PIRNR:PIRNR000355};
KW   Iron {ECO:0000256|PIRNR:PIRNR000355, ECO:0000256|PIRSR:PIRSR000355-2};
KW   Metal-binding {ECO:0000256|PIRNR:PIRNR000355,
KW   ECO:0000256|PIRSR:PIRSR000355-2};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR000355};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199206}.
FT   ACT_SITE        105
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000355-1"
FT   BINDING         67
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000355-2"
FT   BINDING         98
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000355-2"
FT   BINDING         98
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000355-2"
FT   BINDING         101
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000355-2"
FT   BINDING         158
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000355-2"
FT   BINDING         192
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000355-2"
FT   BINDING         195
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000355-2"
SQ   SEQUENCE   351 AA;  40812 MW;  79D46FA0298265F9 CRC64;
     MSLLDARKTY KPFEYPWAYE FWKRQQQVHW LPEEVPLGED CRDWAQKLTH HERNLLTQIF
     RFFTQADVEV QDCYHEKYGR VFKPTEIKMM LAAFSNMETV HIAAYSHLLD TIGMPESEYG
     MFLEYAEMKD KHDYLQKFGV DSDEDIARTL AMFGGFTEGV QLFASFAMLM NFPRFNKMKG
     MGQIVSWSVR DESLHCEGII QLFHTFVKER NCLTKAVKDD IADQCQTTIR LEDAFIDLAF
     EMGPVNGMTP KDIKKYIRYI ADWRMGQLGL KPIYMIDEHP LPWLTPLLNG VEHANFFETR
     ATEYSKAATR GQWSDVWDSF EKRQKAKSVK IANEDAAEEG DMFASAGVAA E
//
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